Recent progress has included the solubilization of alkyl synthase from microsomes using detergents and phospholipase A2 or C. Since this enzyme catalyzes the first committed step in ether bond formation, purification of the alkyl synthase will permit us, for the first time, to assess the unique reaction mechanism that substitutes a long chain fatty alcohol in toto for the acyl group of acyl dihydroxyacetone-P to form the alkyl ether linkage. The properties of alkyl synthase will be characterized an an antibody prepared for use in investigating its regulation and firmly establishing its exact subcellular site. Acyl-CoA reductase (forms the alcohol precursor) and Delta-alkyl desaturase (forms plasmalogens) will be characterized using similar approaches. The ultimate objective is to understand how these three crucial enzymes in the ether lipid pathway function and how they are regulated in cancer cells and glandular tissues that are enriched in ether-linked lipids.